Abstract

Prion proteins that are normal cellular components or involved in pathology can vary little or not at all in primary amino acid sequence, but their glycosylation is different, e.g. in scrapie versus normal forms; in mouse strain-specific isolates; and in BSE (bovine spongiform encephalopathy) and variant CJD (Creutzfeldt–Jakob disease) versus classical CJD. The results of Nielsen et al. published in this issue of the Biochemical Journal show that changes in glycosylation are not restricted to the prion. The paper comprehensively characterizes a decrease in the glycosylation of the insulin receptor in scrapie-infected neuroblastoma cells, but no change in glycosylation of the insulin-like growth factor-1 receptor. Thus the scrapie prion can influence glycosylation, not only of itself, but also of other selected cell glycoproteins.